메뉴 건너뛰기




Volumn 447, Issue 1-3, 2013, Pages 131-139

Rice black-streaked dwarf virus P10 induces membranous structures at the ER and elicits the unfolded protein response in Nicotiana benthamiana

Author keywords

Capsid protein P10; ER membrane modification; ER stress; Rice black streaked dwarf virus; Unfolded protein response

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; LATRUNCULIN B; MEMBRANE PROTEIN; PROTEIN P10;

EID: 84884363106     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2013.09.001     Document Type: Article
Times cited : (49)

References (45)
  • 1
    • 48949107700 scopus 로고    scopus 로고
    • Myosin XI-K is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana
    • Avisar D., Prokhnevsky A.I., Makarova K.S., Koonin E.V., Dolja V.V. Myosin XI-K is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana. Plant Physiol. 2008, 146:1098-1108.
    • (2008) Plant Physiol. , vol.146 , pp. 1098-1108
    • Avisar, D.1    Prokhnevsky, A.I.2    Makarova, K.S.3    Koonin, E.V.4    Dolja, V.V.5
  • 2
    • 79952365639 scopus 로고    scopus 로고
    • Subcellular localization and rearrangement of endoplasmic reticulum by brome mosaic virus capsid protein
    • Bamunusinghe D., Seo J.-K., Rao A.L.N. Subcellular localization and rearrangement of endoplasmic reticulum by brome mosaic virus capsid protein. J. Virol. 2011, 85:2953-2963.
    • (2011) J. Virol. , vol.85 , pp. 2953-2963
    • Bamunusinghe, D.1    Seo, J.-K.2    Rao, A.L.N.3
  • 3
    • 0033932450 scopus 로고    scopus 로고
    • Cowpea mosaic virus infection induces a massive proliferation of endoplasmic reticulum but not Golgi membranes and is dependent on de novo membrane synthesis
    • Carette J.E., Stuiver M., Van Lent J., Wellink J., Van Kammen A. Cowpea mosaic virus infection induces a massive proliferation of endoplasmic reticulum but not Golgi membranes and is dependent on de novo membrane synthesis. J. Virol. 2000, 74:6556-6563.
    • (2000) J. Virol. , vol.74 , pp. 6556-6563
    • Carette, J.E.1    Stuiver, M.2    Van Lent, J.3    Wellink, J.4    Van Kammen, A.5
  • 4
    • 33748502744 scopus 로고    scopus 로고
    • Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
    • Chan C.P., Siu K.L., Chin K.T., Yuen K.Y., Zheng B., Jin D.Y. Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J. Virol. 2006, 80:9279-9287.
    • (2006) J. Virol. , vol.80 , pp. 9279-9287
    • Chan, C.P.1    Siu, K.L.2    Chin, K.T.3    Yuen, K.Y.4    Zheng, B.5    Jin, D.Y.6
  • 5
    • 24644495622 scopus 로고    scopus 로고
    • Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response
    • Chan S.W., Egan P.A. Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response. FASEB J. 2005, 19:1510-1512.
    • (2005) FASEB J. , vol.19 , pp. 1510-1512
    • Chan, S.W.1    Egan, P.A.2
  • 6
    • 0034001930 scopus 로고    scopus 로고
    • Brome mosaic virus polymerase-like protein 2a is directed to the endoplasmic reticulum by helicase-like viral protein 1a
    • Chen J., Ahlquist P. Brome mosaic virus polymerase-like protein 2a is directed to the endoplasmic reticulum by helicase-like viral protein 1a. J. Virol. 2000, 74:4310-4318.
    • (2000) J. Virol. , vol.74 , pp. 4310-4318
    • Chen, J.1    Ahlquist, P.2
  • 7
    • 0028568176 scopus 로고
    • TopPred II: an improved software for membrane protein structure predictions
    • Claros M., von Heijne G. TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 1994, 10:685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.1    von Heijne, G.2
  • 8
    • 33748641937 scopus 로고    scopus 로고
    • Reovirus outer capsid protein μ1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria
    • Coffey C.M., Sheh A., Kim I.S., Chandran K., Nibert M.L., Parker J.S.L. Reovirus outer capsid protein μ1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J. Virol. 2006, 80:8422-8438.
    • (2006) J. Virol. , vol.80 , pp. 8422-8438
    • Coffey, C.M.1    Sheh, A.2    Kim, I.S.3    Chandran, K.4    Nibert, M.L.5    Parker, J.S.L.6
  • 9
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method
    • Cserzö M., Wallin E., Simon I., von Heijne G., Elofsson A. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 1997, 10:673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzö, M.1    Wallin, E.2    Simon, I.3    von Heijne, G.4    Elofsson, A.5
  • 10
    • 79960397172 scopus 로고    scopus 로고
    • Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement
    • Genoves A., Pallas V., Navarro J.A. Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement. J. Virol. 2011, 85:7797-7809.
    • (2011) J. Virol. , vol.85 , pp. 7797-7809
    • Genoves, A.1    Pallas, V.2    Navarro, J.A.3
  • 11
    • 84876425407 scopus 로고    scopus 로고
    • Host endomembrane recruitment for plant RNA virus replication
    • Grangeon R., Jiang J., Laliberté J.F. Host endomembrane recruitment for plant RNA virus replication. Curr. Opin. Virol. 2012, 2:683-690.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 683-690
    • Grangeon, R.1    Jiang, J.2    Laliberté, J.F.3
  • 12
    • 53749085917 scopus 로고    scopus 로고
    • Advances in fluorescent protein-based imaging for the analysis of plant endomembranes
    • Held M.A., Boulaflous A., Brandizzi F. Advances in fluorescent protein-based imaging for the analysis of plant endomembranes. Plant Physiol. 2008, 147:1469-1481.
    • (2008) Plant Physiol. , vol.147 , pp. 1469-1481
    • Held, M.A.1    Boulaflous, A.2    Brandizzi, F.3
  • 13
    • 0000207681 scopus 로고
    • TMBASE - a database of membrane spanning protein segments
    • Hofman K. TMBASE - a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 1993, 374:166-171.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166-171
    • Hofman, K.1
  • 14
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler J.A., Skalet A.H., Alwine J.C. Human cytomegalovirus infection activates and regulates the unfolded protein response. J. Virol. 2005, 79:6890-6899.
    • (2005) J. Virol. , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 15
    • 0031806240 scopus 로고    scopus 로고
    • Detection and assignment of proteins encoded by rice black streaked dwarf fijivirus S7, S8, S9 and S10
    • Isogai M., Uyeda I., Lee B. Detection and assignment of proteins encoded by rice black streaked dwarf fijivirus S7, S8, S9 and S10. J. Gen. Virol. 1998, 79:1487-1494.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1487-1494
    • Isogai, M.1    Uyeda, I.2    Lee, B.3
  • 16
    • 84866309627 scopus 로고    scopus 로고
    • Assembly of the viroplasm by viral non-structural protein Pns10 is essential for persistent infection of rice ragged stunt virus in its insect vector
    • Jia D., Guo N., Chen H., Akita F., Xie L., Omura T., Wei T. Assembly of the viroplasm by viral non-structural protein Pns10 is essential for persistent infection of rice ragged stunt virus in its insect vector. J. Gen. Virol. 2012, 93:2299-2309.
    • (2012) J. Gen. Virol. , vol.93 , pp. 2299-2309
    • Jia, D.1    Guo, N.2    Chen, H.3    Akita, F.4    Xie, L.5    Omura, T.6    Wei, T.7
  • 17
    • 0027551944 scopus 로고
    • Conformational preference functions for predicting helices in membrane proteins
    • Juretić D., Lee B., Trinajstić N., Williams R.W. Conformational preference functions for predicting helices in membrane proteins. Biopolymers 1993, 33:255-273.
    • (1993) Biopolymers , vol.33 , pp. 255-273
    • Juretić, D.1    Lee, B.2    Trinajstić, N.3    Williams, R.W.4
  • 18
  • 19
    • 0029550559 scopus 로고
    • Actomyosin-based motility of endoplasmic reticulum and chloroplasts in Vallisneria mesophyll cells
    • Liebe S., Menzel D. Actomyosin-based motility of endoplasmic reticulum and chloroplasts in Vallisneria mesophyll cells. Biol. Cell 1995, 85:207-222.
    • (1995) Biol. Cell , vol.85 , pp. 207-222
    • Liebe, S.1    Menzel, D.2
  • 20
    • 34249089648 scopus 로고    scopus 로고
    • Rice black-streaked dwarf virus outer capsid protein P10 has self-interactions and forms oligomeric complexes in solution
    • Liu H., Wei C., Zhong Y., Li Y. Rice black-streaked dwarf virus outer capsid protein P10 has self-interactions and forms oligomeric complexes in solution. Virus Res. 2007, 127:34-42.
    • (2007) Virus Res. , vol.127 , pp. 34-42
    • Liu, H.1    Wei, C.2    Zhong, Y.3    Li, Y.4
  • 21
    • 63449094491 scopus 로고    scopus 로고
    • An amphipathic alpha-helix controls multiple roles of brome mosaic virus protein 1a in RNA replication complex assembly and function
    • Liu L., Westler W.M., den Boon J.A., Wang X., Diaz A., Steinberg H.A., Ahlquist P. An amphipathic alpha-helix controls multiple roles of brome mosaic virus protein 1a in RNA replication complex assembly and function. PLoS Pathog. 2009, 5:e1000351.
    • (2009) PLoS Pathog. , vol.5
    • Liu, L.1    Westler, W.M.2    Den Boon, J.A.3    Wang, X.4    Diaz, A.5    Steinberg, H.A.6    Ahlquist, P.7
  • 22
    • 79960408856 scopus 로고    scopus 로고
    • Garlic virus X 11-kDa protein granules move within the cytoplasm and traffic a host protein normally found in the nucleolus
    • Lu Y., Yan F.E.I., Guo W.E.I., Zheng H., Lin L.I.N., Peng J., Adams M.J., Chen J. Garlic virus X 11-kDa protein granules move within the cytoplasm and traffic a host protein normally found in the nucleolus. Mol. Plant Pathol. 2011, 12:666-676.
    • (2011) Mol. Plant Pathol. , vol.12 , pp. 666-676
    • Lu, Y.1    Yan, F.E.I.2    Guo, W.E.I.3    Zheng, H.4    Lin, L.I.N.5    Peng, J.6    Adams, M.J.7    Chen, J.8
  • 23
    • 0028091058 scopus 로고
    • Retention by the endoplasmic reticulum of rotavirus VP7 is controlled by three adjacent amino-terminal residues
    • Maass D., Atkinson P. Retention by the endoplasmic reticulum of rotavirus VP7 is controlled by three adjacent amino-terminal residues. J. Virol. 1994, 68:366-378.
    • (1994) J. Virol. , vol.68 , pp. 366-378
    • Maass, D.1    Atkinson, P.2
  • 24
    • 34548487513 scopus 로고    scopus 로고
    • A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants
    • Nelson B.K., Cai X., Nebenführ A. A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J. 2007, 51:1126-1136.
    • (2007) Plant J. , vol.51 , pp. 1126-1136
    • Nelson, B.K.1    Cai, X.2    Nebenführ, A.3
  • 25
    • 1842457749 scopus 로고    scopus 로고
    • Movement protein of a closterovirus is a type iii integral transmembrane protein localized to the endoplasmic reticulum
    • Peremyslov V.V., Pan Y.-W., Dolja V.V. Movement protein of a closterovirus is a type iii integral transmembrane protein localized to the endoplasmic reticulum. J. Virol. 2004, 78:3704-3709.
    • (2004) J. Virol. , vol.78 , pp. 3704-3709
    • Peremyslov, V.V.1    Pan, Y.-W.2    Dolja, V.V.3
  • 26
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6Å resolution
    • Reinisch K., Nibert M., Harrison S. Structure of the reovirus core at 3.6Å resolution. Nature 2000, 404:960-967.
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.1    Nibert, M.2    Harrison, S.3
  • 27
    • 0030915143 scopus 로고    scopus 로고
    • Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein
    • Schaad M.C., Jensen P.E., Carrington J.C. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J. 1997, 16:4049-4059.
    • (1997) EMBO J. , vol.16 , pp. 4049-4059
    • Schaad, M.C.1    Jensen, P.E.2    Carrington, J.C.3
  • 29
    • 70350109540 scopus 로고    scopus 로고
    • The plant endoplasmic reticulum: a cell-wide web
    • Sparkes I.A., Frigerio L., Tolley N., Hawes C. The plant endoplasmic reticulum: a cell-wide web. Biochem. J. 2009, 423:145-155.
    • (2009) Biochem. J. , vol.423 , pp. 145-155
    • Sparkes, I.A.1    Frigerio, L.2    Tolley, N.3    Hawes, C.4
  • 30
    • 0036223410 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response
    • Su H.L., Liao C.L., Lin Y.L. Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J. Virol. 2002, 76:4162-4171.
    • (2002) J. Virol. , vol.76 , pp. 4162-4171
    • Su, H.L.1    Liao, C.L.2    Lin, Y.L.3
  • 31
    • 84876716117 scopus 로고    scopus 로고
    • The secretory pathway and the actomyosin motility system are required for plasmodesmatal localization of the P7-1 of rice black-streaked dwarf virus
    • Sun Z., Zhang S., Xie L., Zhu Q., Tan Z., Bian J., Sun L., Chen J. The secretory pathway and the actomyosin motility system are required for plasmodesmatal localization of the P7-1 of rice black-streaked dwarf virus. Arch. Virol. 2013, 158:1055-1064.
    • (2013) Arch. Virol. , vol.158 , pp. 1055-1064
    • Sun, Z.1    Zhang, S.2    Xie, L.3    Zhu, Q.4    Tan, Z.5    Bian, J.6    Sun, L.7    Chen, J.8
  • 32
    • 84857195923 scopus 로고    scopus 로고
    • Structural insights into the coupling of virion assembly and rotavirus replication
    • Trask S.D., McDonald S.M., Patton J.T. Structural insights into the coupling of virion assembly and rotavirus replication. Nat. Rev. Microbiol. 2012, 10:165-177.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 165-177
    • Trask, S.D.1    McDonald, S.M.2    Patton, J.T.3
  • 33
    • 84865128828 scopus 로고    scopus 로고
    • Interactions among capsid proteins orchestrate rotavirus particle functions
    • Trask S.D., Ogden K.M., Patton J.T. Interactions among capsid proteins orchestrate rotavirus particle functions. Curr. Opin. Virol. 2012, 2:373-379.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 373-379
    • Trask, S.D.1    Ogden, K.M.2    Patton, J.T.3
  • 34
    • 81255184274 scopus 로고    scopus 로고
    • Rotavirus infection induces the unfolded protein response of the cell and controls it through the nonstructural protein NSP3
    • Trujillo-Alonso V., Maruri-Avidal L., Arias C.F., Lopez S. Rotavirus infection induces the unfolded protein response of the cell and controls it through the nonstructural protein NSP3. J. Virol. 2011, 85:12594-12604.
    • (2011) J. Virol. , vol.85 , pp. 12594-12604
    • Trujillo-Alonso, V.1    Maruri-Avidal, L.2    Arias, C.F.3    Lopez, S.4
  • 35
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady G.E., Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 36
    • 81755174264 scopus 로고    scopus 로고
    • Wrapping membranes around plant virus infection
    • Verchot J. Wrapping membranes around plant virus infection. Curr. Opin. Virol. 2011, 1:388-395.
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 388-395
    • Verchot, J.1
  • 37
    • 0034730318 scopus 로고    scopus 로고
    • A viral movement protein prevents spread of the gene silencing signal in Nicotiana benthamiana
    • Voinnet O., Lederer C., Baulcombe D.C. A viral movement protein prevents spread of the gene silencing signal in Nicotiana benthamiana. Cell 2000, 103:157-167.
    • (2000) Cell , vol.103 , pp. 157-167
    • Voinnet, O.1    Lederer, C.2    Baulcombe, D.C.3
  • 38
    • 0008736038 scopus 로고
    • Organelles involved in the synthesis and transport of hydroxyproline-containing glycoproteins in carrot root discs
    • Wienecke K., Glas R., Robinson D.G. Organelles involved in the synthesis and transport of hydroxyproline-containing glycoproteins in carrot root discs. Planta 1982, 155:58-63.
    • (1982) Planta , vol.155 , pp. 58-63
    • Wienecke, K.1    Glas, R.2    Robinson, D.G.3
  • 39
    • 0031797727 scopus 로고    scopus 로고
    • BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component
    • Xu A., Bellamy A.R., Taylor J.A. BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component. J. Virol. 1998, 72:9865-9872.
    • (1998) J. Virol. , vol.72 , pp. 9865-9872
    • Xu, A.1    Bellamy, A.R.2    Taylor, J.A.3
  • 40
    • 84874730049 scopus 로고    scopus 로고
    • TGBp3 triggers the unfolded protein response and SKP1-dependent programmed cell death
    • Ye C.-M., Chen S., Payton M., Dickman M.B., Verchot J. TGBp3 triggers the unfolded protein response and SKP1-dependent programmed cell death. Mol. Plant Pathol. 2013, 14:241-255.
    • (2013) Mol. Plant Pathol. , vol.14 , pp. 241-255
    • Ye, C.-M.1    Chen, S.2    Payton, M.3    Dickman, M.B.4    Verchot, J.5
  • 41
    • 79958043215 scopus 로고    scopus 로고
    • The unfolded protein response is triggered by a plant viral movement protein
    • Ye C., Dickman M.B., Whitham S.A., Payton M., Verchot J. The unfolded protein response is triggered by a plant viral movement protein. Plant Physiol. 2011, 156:741-755.
    • (2011) Plant Physiol. , vol.156 , pp. 741-755
    • Ye, C.1    Dickman, M.B.2    Whitham, S.A.3    Payton, M.4    Verchot, J.5
  • 42
    • 33750347616 scopus 로고    scopus 로고
    • Characterization of membrane association domains within the tomato ringspot nepovirus X2 protein, an endoplasmic reticulum-targeted polytopic membrane protein
    • Zhang G., Sanfaçon H. Characterization of membrane association domains within the tomato ringspot nepovirus X2 protein, an endoplasmic reticulum-targeted polytopic membrane protein. J. Virol. 2006, 80:10847-10857.
    • (2006) J. Virol. , vol.80 , pp. 10847-10857
    • Zhang, G.1    Sanfaçon, H.2
  • 43
    • 0034888908 scopus 로고    scopus 로고
    • Sequence analysis shows that a dwarfing disease on rice, wheat and maize in china is caused by rice black-streaked dwarf virus
    • Zhang H., Chen J., Lei J., Adams M.J. Sequence analysis shows that a dwarfing disease on rice, wheat and maize in china is caused by rice black-streaked dwarf virus. Eur. J. Plant Pathol. 2001, 107:563-567.
    • (2001) Eur. J. Plant Pathol. , vol.107 , pp. 563-567
    • Zhang, H.1    Chen, J.2    Lei, J.3    Adams, M.J.4
  • 44
    • 84878237457 scopus 로고    scopus 로고
    • Virus-induced ER stress and the unfolded protein response
    • Zhang L., Wang A. Virus-induced ER stress and the unfolded protein response. Front. Plant Sci. 2012, 3:293.
    • (2012) Front. Plant Sci. , vol.3 , pp. 293
    • Zhang, L.1    Wang, A.2
  • 45
    • 24644494132 scopus 로고    scopus 로고
    • Evidence that insertion of tomato ringspot nepovirus NTB-VPg protein in endoplasmic reticulum membranes is directed by two domains: a C-terminal transmembrane helix and an N-terminal amphipathic helix
    • Zhang S.C., Zhang G., Yang L., Chisholm J., Sanfaçon H. Evidence that insertion of tomato ringspot nepovirus NTB-VPg protein in endoplasmic reticulum membranes is directed by two domains: a C-terminal transmembrane helix and an N-terminal amphipathic helix. J. Virol. 2005, 79:11752-11765.
    • (2005) J. Virol. , vol.79 , pp. 11752-11765
    • Zhang, S.C.1    Zhang, G.2    Yang, L.3    Chisholm, J.4    Sanfaçon, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.